• Species Reactivity

  Human

• Specificity

  Detects human EGF R/ErbB1 in direct ELISAs. In direct ELISAs, no cross-reactivity with recombinant human (rh) ErbB2, rhErbB3, or rhErbB4 is observed.

• Source

  Monoclonal Rat IgG    _2A Clone # 423103

• Purification

  Protein A or G purified from hybridoma culture supernatant

• Immunogen

  Mouse myeloma cell line NS0-derived recombinant human EGF R/ErbB1    
  Leu25-Ser645    
  Accession # CAA25240

• Formulation

  Supplied in a saline solution containing BSA and Sodium Azide.

• Label

  Phycoerythrin

Applications

• Recommended    
  Concentration

  Sample

• Flow Cytometry

  10 µL/10    ⁶ cells

  See below

• 
  

Please Note: Optimal dilutions should be determined by each laboratory for each application.  are available in the Technical Information section on our website.

Data Examples

Preparation and Storage

• Shipping

  The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.

• Stability & Storage

  Protect from light.    Do not freeze.    

• 12 months from date of receipt, 2 to 8 °C as supplied.

Background: EGFR

Epidermal Growth Factor Receptor (EGF R), also named erythroblastic leukemia viral oncogene homolog 1 (ErbB1), is a member of the type I receptor tyrosine kinase superfamily. The epidermal growth factor receptor (EGF R) subfamily of receptor tyrosine kinases comprises four members: EGF R (also known as HER1, ErbB1or ErbB), ErbB2 (Neu, HER2), ErbB3 (HER3), and ErbB4 (HER4). All family members are type I transmembrane glycoproteins that have an extracellular domain with two ligand binding cysteine rich domains, separated by a spacer region, and a cytoplasmic domain with a membrane proximal tyrosine kinase domain and a C-terminal tail with multiple tyrosine autophosphorylation sites. The human EGF R geneencodes a 1210 amino acid (aa) residue precursor with a 24 aa putative signal peptide, a 621 aa extracellular domain, a 23 aa transmembrane domain, and a 542 aa cytoplasmic domain. EGF R has been shown to bind a subset of the EGF family ligands, including EGF, amphiregulin, TGF alpha, betacellulin, epiregulin, heparin-binding EGF and neuregulin-2 alpha , in the absence of a coreceptor. Ligand binding induces EGF R homodimerization as well as heterodimerization with ErbB2, resulting in kinase activation, tyrosine phosphorylation and cell signaling. EGF R can also be recruited to form heterodimers with ligand-activated ErbB3 or ErbB4. EGF R signaling has been shown to regulate multiple biological functions including cell proliferation, differentiation, motility and apoptosis. In addition, EGF R signaling has also been shown to play a role in carcinogenesis (1 ‑ 3).

• References:

1. Daly, R.J. (1999) Growth Factors, 16:255.

2. Schlessinger, J. (2000) Cell. 103:211.

3. Maihle, N.J. et al. (2002) Cancer Treat. Res. 107:247.

• Long Name:

  Epidermal Growth Factor Receptor

• Entrez Gene IDs:

  1956 (Human); 13649 (Mouse)

• Alternate Names:

  avian erythroblastic leukemia viral (v-erb-b) oncogene homolog; cell growth inhibiting protein 40; cell proliferation-inducing protein 61; EC 2.7.10; EC 2.7.10.1; EGF R; EGFR; epidermal growth factor receptor (avian erythroblastic leukemia viral (v-erb-b)oncogene homolog); epidermal growth factor receptor; ErbB; ErbB1; ERBB1PIG61; HER1; HER-1; mENA; Proto-oncogene c-ErbB-1; Receptor tyrosine-protein kinase erbB-1